Lanthanum reduces the excitation efficiency in fly photoreceptors

Lanthanum (La3+), a known inhibitor of Ca2+ binding proteins, was applied to the extracellular space of fly retina. Shot noise analysis indicated that a combination of intense light and La3+ caused a large (down to zero) reduction in the rate of occurrence of the quantal responses to single photons (quantum bumps) which sum to produce the photoreceptor potential. Light in the presence of La3+ also increased the effective bump duration. These effects are very similar to the effects of the mutations trp of Drosophila and nss of Lucilia flies on the quantum bump rate and duration. La3+ applied to the nss mutant caused only a small reduction in the bump rate, suggesting that La3+ may affect the nss gene product which is deficient in the mutant. The close similarity in the properties of the receptor potential of the La(3+)-treated photoreceptor of the wild type and of the nss mutant together with existing evidence for the highly reduced intracellular Ca2+ ([Ca2+]i) level in nss photoreceptors suggest that both La3+ and the mutation cause a severe reduction in [Ca2+]i. This effect may arise from an inhibition of a Ca2+ transporter protein located in the surface membrane that normally replenishes Ca2+ pools in the photoreceptors, a process essential for light excitation.     

The function of photostable pigments in fly photoreceptors

The photoreceptors in the fly's ommatidia contain a bistable visual pigment, which can be shifted back and forth by means of light of appropriate wavelengths. The situation is complicated, however, by the presence of photostable pigments. One of them (located in rhabdomeres no. 1–6) absorbs in the UV, another one (in rhabdomeres no. 7y) in the blue spectral range. Such pigments act as (dichroic) colour filters that modify the spectral and polarisation sensitivity of the photoreceptors by means of absorption. It could be shown furthermore that such pigments can also act as sensitizing pigments that modify spectral sensitivities due to sensitization.Based on material presented at the European Neurosciences Meeting, Florence, September 1978     

Temperature and the temporal resolving power of fly photoreceptors

A hot head gives an insect a clearer view of a moving world because warming reduces motion blur by accelerating photoreceptor responses. Over a natural temperature range, 19–34 °C, the speed of response of blowfly (Calliphora vicina) photoreceptors more than doubles, to produce the fastest functional responses recorded from an ocular photoreceptor. This acceleration increases temporal resolving power, as indicated by the corner frequency of the response power spectrum. When light adapted, the corner frequency increases from 53 Hz to 119 Hz with a Q ₁₀ of 1.9, and when dark adapted from 8 Hz to 32 Hz with a Q ₁₀ of 3.0. Temperature sensitivity originates in the phototransduction cascade, and is associated with signal amplification. The temperature sensitivity of photoreceptors must be taken into account when studying the mechanisms, function and ecology of vision, and gives a distinct advantage to insects that thermoregulate. Accepted: 2 February 2000     

Spectral sensitivity of photoreceptors in the compound eye of the locust

Three types of receptor with different _max of 360, 430, and 530 nm were found in the locust retina by extracellular recording. Their spectral sensitivity curves were considerably broader than the absorption curves of the corresponding pigments. Possible coefficients of electrical coupling between different receptor types in ommatidia were calculated on the basis of the spectral sensitivity curves obtained for photoreceptors, assuming that each receptor contains only one light-sensitive pigment. The resulting values resembled coefficients measured in the locust by Shaw and Lillywhite. The way in which spectral sensitivity curves spread in comparison with pigment absorption curves may thus be caused by electrical coupling between cells.Institute of Problems in Information Transmission, Academy of Sciences of the USSR, Moscow. Translated from Neirofiziologiya, Vol. 18, No. 1, pp. 69–76, January–February, 1986.     

Protection against photodestruction in fly photoreceptors by carotenoid pigments

Summary Microspectrophotometry has shown that fly rhabdomeres with C₄₀-carotenoid pigments incorporated into their membrane are more resistant to destruction by short wavelength radiation than others, lacking this pigment (Kirschfeld 1982). We show here that the fine structure of those photoreceptors with the carotenoids is also much better preserved after uv-illumination than in cells lacking this pigment. The intensity of uv-illumination in the experiments was higher than in natural conditions in order to enhance the observable effects, but it is concluded that carotenoid pigments in photoreceptors should also serve a protective function under normal conditions.     

The influence of extracellular calcium on the response of fly photoreceptors

Summary This paper presents a systematic investigation of the influence of the extracellular concentration of calcium ([Ca²⁺]₀) on the electrophysiological response of the fly's photoreceptors (R1–R6) to light. The hemisected heads of flies were perfused with a standard medium containing 10^–4 mol/1 CaCl₂ and in this medium the intracellularly recorded response of the cell was virtually identical to the normal response obtained in vivo. All the effects of changing the [Ca²⁺]₀ could be reversed within 5 min by perfusing the eye with the standard medium.Changing the [Ca²⁺]₀ did not influence the frequency with which quantum bumps occurred or the resting membrane potential, but did lead to changes in the latency and amplitude of the response and, most significantly, in the repolarization time (t _r). The plot oft _r versus the [Ca²⁺]₀ revealed that the value oft _r changes significantly in two distinct regions representing a [Ca²⁺]₀ of between 2×10^–8 and 10^–7 mol/l and 10^–4 and 10^–2 mol/l, respectively. Lowering the [Ca²⁺]₀ did not affect the amplitude of the response but did lead to a drastic increase int _r which was accompanied by an increase in latency and peak time. Raising the [Ca²⁺]₀ led to a reduction in the duration and amplitude of the response. The latter effect is evidence of reduction in the sensitivity of the photoreceptor cell which is dependent on the [Ca²⁺]₀.It is postulated that two types of binding site for calcium exist, high affinity binding sites (HABS) and low affinity binding sites (LABS), which modulate the functioning of ion channels in the cell membrane that are activated as a consequence of light absorption. The results indicate that the sensitivity of the photoreceptor cell is determined by the degree of saturation of the LABS.     

Spectral sensitivity of photoreceptors in the compound eye of stingless tropical bees

The spectral sensitivity of photoreceptors of the tropical bees Melipona quadrifasciata, M. marginata, and Trigona spinipes were measured on-line with a rapid constant response amplitude method. The results indicate that although these bees forage in different habitats they have the same set of photoreceptors with sensitivity maxima in ultra-violet, blue and green.     

Linear behaviour in the aperture pupil of single photoreceptors: Consequences related to the degree of inhomogeneity

An exact treatment of the initial field falling on the entrance face of a photoreceptor, so that the scattered field far from the latter vanishes, is presented. Its physical interest and some consequences are discussed. By establishing certain similarities between the behaviour of the photoreceptor as light penetrates into and propagates along, and an optical linear system, it is possible to define a spatial transverse impulse response containing information on the diffraction capability of each individual receptor. The distribution of this function across a transverse plane depends upon the particular form of the refractive index in the photoreceptor. Thus, certain differences are seen to occur between the case of an homogeneous receptor and an inhomogeneous one, for particular values in the degree of inhomogeneity. This fact allows to interpret the presence of inhomogeneities in the photoreceptor structure.     

Chemical excitation and inactivation in photoreceptors of the fly mutants trp and nss

The Drosophila and Lucilia photoreceptor mutants, trp and nss, respond like wild-type flies to a short pulse of intense light or prolonged dim light; however, upon continuous intense illumination, the trp and nss mutants are unable to maintain persistent excitation. This defect manifests itself by a decline of the receptor potential toward baseline during prolonged intense illumination with little change in the shape or amplitude of the quantal responses to single photons (quantum bumps). Previous work on the trp and nss mutants suggests that a negative feedback loop may control the rate of bump production. Chemical agents affecting different steps of the phototransduction cascade were used in conjunction with light to identify a possible branching point of the feedback loop and molecular stages which are affected by the mutation. Fluoride ions, which in the dark both excite and adapt the photoreceptors of wild-type flies, neither excite nor adapt the photoreceptors of the trp and nss mutants. The hydrolysis-resistant analogue, GTP gamma S, which excites the photoreceptors of wild-type flies, resulting in noisy depolarization, markedly reduces the light response of both mutant flies. Intracellular recordings revealed, however, that the inhibitory effect of GTP gamma S on the nss mutant was accompanied neither by any significant depolarization nor by an increase in the noise, and thus was very different from the effect of a dim background light. The combination of inositol trisphosphate and diphosphoglycerate (InsP3 + DPG), which efficiently excites the photoreceptors of wild-type Lucilia, also excites the photoreceptors of nss Lucilia mutant. The InsP3 + DPG together act synergistically with light to accelerate the decline of the response to light in the mutant flies. These results suggest that the fly phototransduction pathway involves a feedback regulatory loop, which branches subsequent to InsP3 production and regulates guanine nucleotide-binding protein (G protein)-phospholipase C activity. A defect in this regulatory loop, which may cause an unusually low level of intracellular Ca2+, severely reduces the triggering of bumps in the mutants during intense prolonged illumination.     

Distinct functions of neuronal synaptobrevin in developing and mature fly photoreceptors

Neuronal synaptobrevin (n-Syb, alias VAMP2), a synaptic vesicle membrane protein with a central role in neurotransmission, is specifically cleaved by the light chain of tetanus neurotoxin (TNT) that is known to reliably block neuroexocytosis. Here, we study fly photoreceptors transmitting continuous, graded signals to first order interneurons in the lamina, and report consequences of targeted expression of TNT in these cells using the UAS/GAL4 driver/effector system. Expressing the toxin throughout photoreceptor development causes developmental, electrophysiological, and behavioral defects. These can be differentiated by confining toxin expression to shorter developmental periods. Applying a method for controlled temporal and spatial TNT expression, we found that in the early pupa it impaired the development of the retina; in the midpupa, during synapse formation TNT caused a severe hypoplasia of the lamina that persisted into adulthood and left the photoreceptor-interneuron synapses of the lamina without function. Finally, during adulthood TNT neither blocks synaptic transmission in photoreceptors nor depletes the cells of n-Syb. Our study suggests a novel, cell type-specific function of n-Syb in synaptogenesis and it distinguishes between two synapse types: TNT resistant and TNT sensitive ones. These results need to be taken into account if TNT is used for neural circuit analysis.     

Regulation of light-dependent Gqalpha translocation and morphological changes in fly photoreceptors

Heterotrimeric G-proteins relay signals between membrane-bound receptors and downstream effectors. Little is known, however, about the regulation of Galpha subunit localization within the natural endogenous environment of a specialized signaling cell. Here we show, using live Drosophila flies, that light causes massive and reversible translocation of the visual Gqalpha to the cytosol, associated with marked architectural changes in the signaling compartment. Molecular genetic dissection together with detailed kinetic analysis enabled us to characterize the translocation cycle and to unravel how signaling molecules that interact with Gqalpha affect these processes. Epistatic analysis showed that Gqalpha is necessary but not sufficient to bring about the morphological changes in the signaling organelle. Furthermore, mutant analysis indicated that Gqbeta is essential for targeting of Gqalpha to the membrane and suggested that Gqbeta is also needed for efficient activation of Gqalpha by rhodopsin. Our results support the 'two-signal model' hypothesis for membrane targeting in a living organism and characterize the regulation of both the activity-dependent Gq localization and the cellular architectural changes in Drosophila photoreceptors.     

Angular and spectral sensitivity of fly photoreceptors. III. Dependence on the pupil mechanism in the blowfly<Emphasis Type="Italic"> Calliphora</Emphasis>

A wave optics model for the facet lens-rhabdomere system of fly eyes is used to analyze the dependence of the angular and spectral sensitivity of R1–6 photoreceptors on the pupil mechanism. This assembly of light-absorbing pigment granules in the soma interacts with the waveguide modes propagating in the rhabdomere. A fly rhabdomere carries two modes in the middle wavelength range and four modes at short wavelengths, depending on the rhabdomere diameter and the angle of the incident light flux. The extension of the mode to outside the rhabdomere strongly depends on wavelength, and this dependence plays a determinant role in the light control function of the pupil. The absorbance spectrum of the pigment in the pupil granules is severely depressed at short wavelengths by waveguide effects, resulting in a distinct blue peak. Accordingly, pupil closure suppresses the photoreceptors spectral sensitivity much more in the blue-green than in the UV. The pupil only narrows the angular sensitivity at short wavelengths. The geometrical size of the rhabdomere governs the angular sensitivity of fly photoreceptors in the dark-adapted state, but diffraction takes over in the fully light-adapted state.